Jun 9, 2020Paper

Structural modeling of 2019-novel coronavirus (nCoV) spike protein reveals a proteolytically-sensitive activation loop as a distinguishing feature compared to SARS-CoV and related SARS-like coronaviruses

BioRxiv : the Preprint Server for Biology
Javier A JaimesGary R Whittaker

Abstract

The 2019 novel coronavirus (2019-nCoV) is currently causing a widespread outbreak centered on Hubei province, China and is a major public health concern. Taxonomically 2019-nCoV is closely related to SARS-CoV and SARS-related bat coronaviruses, and it appears to share a common receptor with SARS-CoV (ACE-2). Here, we perform structural modeling of the 2019-nCoV spike glycoprotein. Our data provide support for the similar receptor utilization between 2019-nCoV and SARS-CoV, despite a relatively low amino acid similarity in the receptor binding module. Compared to SARS-CoV, we identify an extended structural loop containing basic amino acids at the interface of the receptor binding (S1) and fusion (S2) domains, which we predict to be proteolytically-sensitive. We suggest this loop confers fusion activation and entry properties more in line with MERS-CoV and other coronaviruses, and that the presence of this structural loop in 2019-nCoV may affect virus stability and transmission.

Citations

Jun 18, 2020·Journal of Virology·Noton K DuttaJames T Gordy
May 20, 2020·Journal of Zhejiang University. Science. B·Yu ShiZhi Chen
Mar 12, 2020·Nature·Smriti Mallapaty
Aug 28, 2020·Frontiers in Cellular Neuroscience·Matija FenrichMarija Heffer
Jun 14, 2020·Signal Transduction and Targeted Therapy·Bin ChenWei Cheng
Dec 2, 2020·Annals of Clinical Microbiology and Antimicrobials·Hussain A SafarTimothy D McHugh

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